Superoxide radical and superoxide dismutases.

@article{Fridovich1995SuperoxideRA,
  title={Superoxide radical and superoxide dismutases.},
  author={Irwin Fridovich},
  journal={Annual review of biochemistry},
  year={1995},
  volume={64},
  pages={
          97-112
        }
}
  • I. Fridovich
  • Published 1995
  • Biology, Chemistry
  • Annual review of biochemistry
O2- oxidizes the [4Fe-4S] clusters of dehydratases, such as aconitase, causing-inactivation and release of Fe(II), which may then reduce H2O2 to OH- +OH.. SODs inhibit such HO. production by scavengingO2-, but Cu, ZnSODs, by virtue of a nonspecific peroxidase activity, may peroxidize spin trapping agents and thus give the appearance of catalyzing OH. production from H2O2. There is a glycosylated, tetrameric Cu, ZnSOD in the extracellular space that binds to acidic glycosamino-glycans. It… 
Use of recombinant iron-superoxide dismutase as a marker of nitrative stress.
Bicarbonate Is Required for the Peroxidase Function of Cu,Zn-Superoxide Dismutase at Physiological pH*
TLDR
A comprehensive EPR investigation of the radical production and redox state of the active site copper was performed, and data suggest that HCO3 − bound to Arg141 anchors the neutral H2O2molecule at theactive site copper, enabling its redox cleavage.
Peroxynitrite-induced nitration of tyrosine-34 does not inhibit Escherichia coli iron superoxide dismutase.
TLDR
The pK(a) of nitrated tyrosine-34 was determined to be 7.95+/-0.15, indicating that the peroxynitrite-modified enzyme appreciably maintains its protonation state under physiological conditions.
Superoxide: a two-edged sword.
  • B. Babior
  • Chemistry
    Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas
  • 1997
Superoxide (O2-) is the compound obtained when oxygen is reduced by one electron. For a molecule with an unpaired electron, O2- is surprisingly inert, its chief reaction being a dismutation in which
Peroxynitrite-induced nitration of tyrosine-34 does not inhibit Escherichia coli iron superoxide dismutase
TLDR
The pK(a) of nitrated tyrosine-34 was determined to be 7.95+/-0.15, indicating that the peroxynitrite-modified enzyme appreciably maintains its protonation state under physiological conditions.
Divalent-metal-dependent nucleolytic activity of Cu, Zn superoxide dismutase
TLDR
It is revealed that the divalent-metal-dependent DNA cleavage activity is an intrinsic property of the holo SOD, which is independent of its natural metal sites, and may provide an alternative insight into the link between SOD enzymes and neurodegenerative disorders.
Evidence against the Generation of Free Hydroxyl Radicals from the Interaction of Copper,Zinc-Superoxide Dismutase and Hydrogen Peroxide*
TLDR
A comprehensive EPR investigation of radical production and the kinetics of spin trapping was performed in the presence of a series of structurally different⋅OH scavengers, finding that characteristic radicals formed by peroxidases were also efficiently generated by H2O2 and SOD.
Superoxide dismutase : An alternate target for Plasmodium
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This study shows that the PfFeSOD is different from cytosolic Cu-ZnSOD1 of H. sapiens which is likely to be found in the erythrocytes, with just five conserved residues, and could be an ideal enzyme to target anti-malarials for this parasite.
Superoxide-Driven Aconitase FE–S Center Cycling
O-2 produced by the autoxidation of respiratory chain electron carriers, and other cellular reductants, inactivates bacterial and mammalian iron-sulfur-containing (de)hydratases including the citric
Superoxide does react with peroxides: direct observation of the Haber-Weiss reaction in the gas phase.
TLDR
The fact that nature provides specific enzymes to selectively remove superoxide from aerobic organisms, namely, the superoxide dismutase enzymes, suggests that superoxide itself is relatively unreactive toward most cellular components, which suggests that dismut enzyme enzymes may ultimately protect the cell against more pernicious oxidants formed from superoxide.
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TLDR
The demonstration that O2·- can reduce ferricytochrome c and tetranitromethane, and that superoxide dismutase, by competing for the superoxide radicals, can markedly inhibit these reactions, is demonstrated.
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TLDR
It can be deduced that the autoxidation of ferrocytochrome c, under a variety of conditions, geenerates O2 minus which can then dismute to H202 + O2 or can reduce ferricy tochrome c back to ferroCytochromec.
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TLDR
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